ID A0A1B2HGD6_9PSEU Unreviewed; 584 AA.
AC A0A1B2HGD6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:ANZ36781.1};
GN ORFNames=BBK82_12590 {ECO:0000313|EMBL:ANZ36781.1};
OS Lentzea guizhouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=1586287 {ECO:0000313|EMBL:ANZ36781.1, ECO:0000313|Proteomes:UP000093053};
RN [1] {ECO:0000313|EMBL:ANZ36781.1, ECO:0000313|Proteomes:UP000093053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHS C013 {ECO:0000313|EMBL:ANZ36781.1,
RC ECO:0000313|Proteomes:UP000093053};
RA Cao C.;
RT "Complete genome sequence of the Lentzea guizhouensis DHS C013.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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DR EMBL; CP016793; ANZ36781.1; -; Genomic_DNA.
DR RefSeq; WP_065915180.1; NZ_CP016793.1.
DR AlphaFoldDB; A0A1B2HGD6; -.
DR STRING; 1586287.BBK82_12590; -.
DR KEGG; led:BBK82_12590; -.
DR Proteomes; UP000093053; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR NCBIfam; TIGR00666; PBP4; 1.
DR PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 2.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:ANZ36781.1};
KW Hydrolase {ECO:0000313|EMBL:ANZ36781.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:ANZ36781.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000093053};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 60525 MW; 07AC3A0812442555 CRC64;
MDQRCGDQAW PYAQRKEPQH HEPLTRQDLQ RPSQRHAPAA LHQNGSHQNG QQNGHQNGAH
QNGAAQRPDL THPETVRIAP VQRPPQHQPK RAEEPKELPG HDEELEDRLT EAKPKTKTHT
DTEPDTEPET DQPKKTRKPL AIALAVLVVA ALTGATIFAV NEFSGQAAVE TKPPAAPVDV
QPLVKPASAQ GTAPTPQGVQ RALAGPAGSG ALGTLTGSVV DPATGTVLWQ QGDTNPATPA
SSLKVLTAAA ALLELDKTAQ LSTKVVRGAE PGTVVIIGGG DPTISATPGS SVYPGAAQLD
DLVNQVRQQG PVTKVLYDLG RYAGEQMGPQ WETVDIAGGS VAPIVPFMVD GGRLDPRKVE
VARTPNPAQQ AADAFAARLG ATAAPGVAPP GAQTIAEVKS ASIEQLVDNM MQISDNVLTE
AVARELAIKT GNEPSFAGGV KAVRETLTKH GFDLSGASFV DGSGLSATNK IPAKLLTDVL
MAAAKPALDD RTAKLRPLLT SLPVAGGSGT LAGRYGGVAA QGKGWVRAKT GTLTGVNALA
GVVVDEDGRV LVFAFMSASP GNPETEVRPA LDVLATALRG CGCS
//
